Evidence map›Paper›PMID 32556937›Full record

ReviewNeurotoxicity research2020

Exploring the Role of PSEN Mutations in the Pathogenesis of Alzheimer's Disease.

Md Tanvir Kabir, Md Sahab Uddin, Jinnat Ruksana Setu, Ghulam Md Ashraf, May N Bin-Jumah, Mohamed M Abdel-Daim

Abstract readReview
PubMed Publisher
In one paragraph

Review in Neurotoxicity research, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
3.7field-weighted citation impact, top 6% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

41 citing papers in PubMed, 61 citations in OpenAlex.

  1. Article
  2. NovelWorld journal of radiology · 2026
    Article
  3. ZL006 Treatment Reduces Inflammation, Oxidative Stress, and Brain AβInternational journal of molecular sciences · 2026
    Article
  4. Article
  5. Autophagy-lysosomal pathway in neurodegeneration.Molecular neurodegeneration advances · 2026
    Review
  6. Review
  7. Review
  8. Article
  9. Review
  10. Article
  11. Reevaluating the role of amyloidFrontiers in neurology · 2025
    Review
  12. Review
  13. Review
  14. Article
  15. Article
  16. Review
  17. Review
  18. Review
  19. Deciphering the Role of Selenoprotein M.Antioxidants (Basel, Switzerland) · 2023
    Review
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 6 institutions in 3 countries.

Md Tanvir KabirDepartment of Pharmacy, Brac University, Dhaka, Bangladesh.
Md Sahab UddinDepartment of Pharmacy, Southeast University, Dhaka, Bangladesh. msu-neuropharma@hotmail.com.ORCID https://orcid.org/0000-0002-0805-7840
Jinnat Ruksana SetuDepartment of Pharmacy, Southeast University, Dhaka, Bangladesh.
Ghulam Md AshrafKing Fahd Medical Research Center, King Abdulaziz University, Jeddah, Saudi Arabia.
May N Bin-JumahDepartment of Biology, College of Science, Princess Nourah bint Abdulrahman University, Riyadh, 11474, Saudi Arabia.
Mohamed M Abdel-DaimDepartment of Zoology, College of Science, King Saud University, P.O. Box 2455, Riyadh, 11451, Saudi Arabia.
BRAC University · BDKing Abdulaziz University · SAPrincess Nourah bint Abdulrahman University · SASoutheast University · BDSuez Canal University · EGUttara University · BD

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Alzheimer's disease (AD) is the most common cause of dementia. Mutations of presenilin (PSEN) genes that encode presenilin proteins have been found as the vital causal factors for early-onset familial AD (FAD). AD pathological features such as memory loss, synaptic dysfunction, and formation of plaques have been successfully mimicked in the transgenic mouse models that coexpress FAD-related presenilin and amyloid precursor protein (APP) variants. γ-Secretase (GS) is an enzyme that plays roles in catalyzing intramembranous APP proteolysis to release pathogenic amyloid beta (Aβ). It has been found that presenilins can play a role as the GS's catalytic subunit. FAD-related mutations in presenilins can modify the site of GS cleavage in a way that can elevate the production of longer and highly fibrillogenic Aβ. Presenilins can interact with β-catenin to generate presenilin complexes. Aforesaid interactions have also been studied to observe the mutational and physiological activities in the catenin signal transduction pathway. Along with APP, GS can catalyze intramembrane proteolysis of various substrates that play a vital role in synaptic function. PSEN mutations can cause FAD with autosomal dominant inheritance and early onset of the disease. In this article, we have reviewed the current progress in the analysis of PSENs and the correlation of PSEN mutations and AD pathogenesis.

Indexed as

Alzheimer DiseaseAnimalsHumansMutationPresenilin-1Presenilin-2ProteolysisSignal TransductionPresenilin-1Presenilin-2PSEN1 protein, humanPSEN2 protein, humanAlzheimer’s diseaseAmyloid betaPresenilinPSENγ-Secretase

Identifiers

PMID32556937
OpenAlexW3035913979

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.